Protein profile
PA1546
oxygen-independent coproporphyrinogen-III oxidase
Genome: NC_002516.2
Overview
Basic information about this protein and its source genome.
- Accession
- PA1546
- Gene
- hemN PA1546
- Status
- annotated
- Amino acids
- 460
- Structure source
- AlphaFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- hit
- Human identity (%)
- 30.645
- Human E-value
- 4.3e-20
- Gut microbiome off-target
- hit
- Essential (DEG)
- Y
- Localization
- Cytoplasmic
Selected Druggability evidence
Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Enzyme Commission (EC)
1Gene Ontology (GO)
9- GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
- GO:0051539 Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
- GO:0051989 Catalysis of the reaction: coproporphyrinogen III + 2 S-adenosyl-L-methionine = protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine.
- GO:0004109 Catalysis of the reaction: coproporphyrinogen III + 2 H+ + O2 = 2 CO2 + 2 H2O + protoporphyrinogen IX.
- GO:0046872 Binding to a metal ion.
- GO:0006779 The chemical reactions and pathways resulting in the formation of any member of a large group of derivatives or analogs of porphyrin. Porphyrin consists of a ring of four pyrrole nuclei linked each to the next at their alpha positions through a methine group.
- GO:0006782 The chemical reactions and pathways resulting in the formation of protoporphyrinogen IX.
- GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
- GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 63 | 255 | CDD | cd01335 | Radical_SAM |
| 14 | 448 | PANTHER | PTHR13932 | COPROPORPHYRINIGEN III OXIDASE |
| 14 | 448 | InterPro | IPR034505 | Anaerobic coproporphyrinogen-III oxidase |
| 53 | 276 | SMART | SM00729 | MiaB |
| 53 | 276 | InterPro | IPR006638 | Elp3/MiaA/NifB-like, radical SAM core domain |
| 61 | 284 | Gene3D | G3DSA:3.80.30.20 | tm_1862 like domain |
| 61 | 284 | InterPro | IPR023404 | Radical SAM, alpha/beta horseshoe |
| 3 | 460 | SFLD | SFLDG01065 | anaerobic coproporphyrinogen-III oxidase like |
| 63 | 254 | SFLD | SFLDG01082 | B12-binding domain containing |
| 368 | 460 | FunFam | G3DSA:1.10.10.920:FF:000002 | Coproporphyrinogen-III oxidase |
| 5 | 448 | SUPERFAMILY | SSF102114 | Radical SAM enzymes |
| 3 | 459 | PIRSF | PIRSF000167 | HemN |
| 3 | 459 | InterPro | IPR004558 | Oxygen-independent coproporphyrinogen III oxidase HemN |
| 6 | 460 | NCBIfam | TIGR00538 | oxygen-independent coproporphyrinogen III oxidase |
| 6 | 460 | InterPro | IPR004558 | Oxygen-independent coproporphyrinogen III oxidase HemN |
| 3 | 460 | SFLD | SFLDF00277 | oxygen-independent coproporphyrinogen-III oxidase 1 (HemN-like) |
| 3 | 460 | InterPro | IPR004558 | Oxygen-independent coproporphyrinogen III oxidase HemN |
| 58 | 232 | Pfam | PF04055 | Radical SAM superfamily |
| 58 | 232 | InterPro | IPR007197 | Radical SAM |
| 368 | 460 | Gene3D | G3DSA:1.10.10.920 | - |
| 48 | 287 | ProSiteProfiles | PS51918 | Radical SAM core domain profile. |
| 48 | 287 | InterPro | IPR007197 | Radical SAM |
| 369 | 435 | Pfam | PF06969 | HemN C-terminal domain |
| 369 | 435 | InterPro | IPR010723 | HemN, C-terminal |
3D Structure
Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.
Loading 3D structure...
Structural evidence
0 + 1Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
PA1546
|
AlphaFold | — | — | full sequence | — | Viewing |
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer
Pockets (FPOCKET)
Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).
| FPOCKET | Sticks | Spheres | Surfaces | Druggability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|
| 1 | 0.616 | ||||||
| 2 | 0.502 |